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Vol 52(2018) N 2 p. 137-150; DOI 10.1134/S0026893317050028 Full Text

K.A. Akhmetova1,2,3, I.N. Chesnokov2, S.A. Fedorova1,3*

Functional Characterization of Septin Complexes

1Institute of Cytology and Genetics, Siberian Branch of the Russian Academy of Sciences, Novosibirsk, 630090 Russia
2University of Alabama at Birmingham, Birmingham, 35294 USA
3Novosibirsk National Research State University, Novosibirsk, 630090 Russia

*fsveta@bionet.nsc.ru
Received - 2016-07-11; Accepted - 2016-10-27

Septins belong to a family of conserved GTP-binding proteins found in majority of eukaryotic species except for higher plants. Septins form nonpolar complexes that further polymerize into filaments and associate with cell membranes, thus comprising newly acknowledged cytoskeletal system. Septins participate in a variety of cell processes and contribute to various pathophysiological states, including tumorigenesis and neurodegeneration. Here, we review the structural and functional properties of septins and the regulation of their dynamics with special emphasis on the role of septin filaments as a cytoskeletal system and its interaction with actin and microtubule cytoskeletons. We also discuss how septins compartmentalize the cell by forming local protein-anchoring scaffolds and by providing barriers for the lateral diffusion of the membrane proteins.

septins, septin complexes, septin filaments, septin scaffold



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